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The growing usage of nanoparticles of zinc sulfide as quantum dots andbiosensors calls for a theoretical assessment of interactions of ZnS withbiomolecules. We employ the molecular-dynamics-based umbrella sampling methodto determine potentials of mean force for 20 single amino acids near the ZnS(110) surface in aqueous solutions. We find that five amino acids do not bindat all and the binding energy of the remaining amino acids does not exceed 4.3kJ/mol. Such energies are comparable to those found for ZnO (and to hydrogenbonds in proteins) but the nature of the specificity is different. Cysteine canbind with ZnS in a covalent way, e.g. by forming the disulfide bond with S inthe solid. If this effect is included within a model incorporating the Morsepotential, then the potential well becomes much deeper - the binding energy isclose to 98 kJ/mol. We then consider tryptophan cage, a protein of 20 residues,and characterize its events of adsorption to ZnS. We demonstrate the relevanceof interactions between the amino acids in the selection of optimal adsorbedconformations and recognize the key role of cysteine in generation of lastingadsorption. We show that ZnS is more hydrophobic than ZnO and that the densityprofile of water is quite different than that forming near ZnO - it has only aminor articulation into layers. Furthermore, the first layer of water isdisordered and mobile.

Interactions of aqueous amino acids and proteins with the (110) surface of ZnS in molecular dynamics simulations